The hydrophobic, membrane-bound form of Torpedo acetylcholinesterase is specifically solubilized by a phosphatidylinositol-specific phospholipase C, suggesting that acetylcholinesterase is bound to the membrane via a direct and specific interaction with phosphatidylinositol (Futerman et al., Biochem. J. (1985) 226, 369-377). Here we demonstrate the presence of covalently bound inositol in the membrane-anchoring domain of purified Torpedo acetylcholinesterase. Upon removal of this domain, levels of inositol are reduced to only 15-20% of those found in the intact enzyme.
        
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Futerman AH, Low MG, Ackermann KE, Sherman WR, Silman I (1985) Identification of covalently bound inositol in the hydrophobic membrane-anchoring domain of Torpedo acetylcholinesterase Biochemical & Biophysical Research Communications129: 312-7
Futerman AH, Low MG, Ackermann KE, Sherman WR, Silman I (1985) Biochemical & Biophysical Research Communications129: 312-7